ID A0A069DA45_9BACL Unreviewed; 645 AA.
AC A0A069DA45;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Myo-inositol catabolism protein IolD {ECO:0000313|EMBL:GAK39251.1};
GN ORFNames=TCA2_1739 {ECO:0000313|EMBL:GAK39251.1};
OS Paenibacillus sp. TCA20.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1499968 {ECO:0000313|EMBL:GAK39251.1, ECO:0000313|Proteomes:UP000028160};
RN [1] {ECO:0000313|EMBL:GAK39251.1, ECO:0000313|Proteomes:UP000028160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCA20 {ECO:0000313|EMBL:GAK39251.1,
RC ECO:0000313|Proteomes:UP000028160};
RA Fujinami S., Takeda-Yano K., Onodera T., Satoh K., Sano M., Takahashi Y.,
RA Narumi I., Ito M.;
RT "Draft Genome Sequence of Calcium-Dependent Paenibacillus sp. Strain TCA20,
RT Isolated from a Hot Spring Containing a High Concentration of Calcium
RT Ions.";
RL Genome Announc. 2:e00866-14(2014).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAK39251.1}.
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DR EMBL; BBIW01000002; GAK39251.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A069DA45; -.
DR eggNOG; COG3962; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000028160; Unassembled WGS sequence.
DR GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0019310; P:inositol catabolic process; IEA:InterPro.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR030817; Myo_inos_IolD.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR04377; myo_inos_iolD; 1.
DR PANTHER; PTHR18968:SF9; 3D-(3,5/4)-TRIHYDROXYCYCLOHEXANE-1,2-DIONE HYDROLASE; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000028160};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..132
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 219..353
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 442..600
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 645 AA; 70113 MW; C2C9301834C851C3 CRC64;
MTKIRMTTAQ ALIKFLNQQF IETKSGTQRF VQGIFTVFGH GNVLGLGQAL ESDSGELTAY
QGRNEQGMAH AAMAFAKQNN RRQIMACTAS IGPGSANMLT AAATATANQI PVLLLPSDTF
ASRQPDPVLQ QMEHTYSAAI TVNDAFKSVC KYWDRVSRPE QLMAAMLNAM RVLTDPADTG
AVAISLPQDV QGEAWEYPES FFQKRIHRIE RRLPHPRDIT EAADLIIQKC KPVIICGGGV
RYSGAGIALK TFAEKFGVPF AETQAGKSAV ESSHAYNLGG IGVTGNAAAN KLASEADLII
GIGTRFTDFT TGSKSLFRNP EVEFITLNAS SFHASKLDAT AVVCDAAEGL DALTSALAER
SYQTSPDYQD EISAVKSEWR RERMRLAEVE YSAEGFMPEI AGHLDEKLAE YAGALGSTLT
QTRVLAVVND MIPNDAIVVG AAGSLPGDMQ RMWENTVTDT YHMEYGFSCM GYEIAGALGV
KLAEPDREVY ALVGDGSYQM LHSELVTSLQ EQKKINIILL DNGGFGCINN LQMEHGMSSI
GTEFRYRGSD GTLNDKLMAI DYAASAAGYG AVTYRVTSIE ELKAAIRDAR LQNVSTLIDV
KVLPKTMTHG YGSWWHVGVA EETDSDTVRA AHKRKLQGLE RARLY
//